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Database: UniProt
Entry: A0A0D3A6W5_BRAOL
LinkDB: A0A0D3A6W5_BRAOL
Original site: A0A0D3A6W5_BRAOL 
ID   A0A0D3A6W5_BRAOL        Unreviewed;       813 AA.
AC   A0A0D3A6W5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN   Name=106312144 {ECO:0000313|EnsemblPlants:Bo1g048170.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g048170.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo1g048170.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo1g048170.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   RefSeq; XP_013605001.1; XM_013749547.1.
DR   AlphaFoldDB; A0A0D3A6W5; -.
DR   STRING; 109376.A0A0D3A6W5; -.
DR   EnsemblPlants; Bo1g048170.1; Bo1g048170.1; Bo1g048170.
DR   GeneID; 106312144; -.
DR   Gramene; Bo1g048170.1; Bo1g048170.1; Bo1g048170.
DR   KEGG; boe:106312144; -.
DR   eggNOG; ENOG502R6BG; Eukaryota.
DR   HOGENOM; CLU_000288_116_5_1; -.
DR   OMA; IWYNEIS; -.
DR   OrthoDB; 501776at2759; -.
DR   Proteomes; UP000032141; Chromosome C1.
DR   ExpressionAtlas; A0A0D3A6W5; baseline.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblPlants.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0060320; P:rejection of self pollen; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF219; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF11883; DUF3403; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000641}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..813
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002256431"
FT   TRANSMEM        437..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..149
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          342..425
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          499..785
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   813 AA;  91817 MW;  CD78B47A7C7A1D7C CRC64;
     MRKIPSMFWV PLFLLSSSFS VALDYSVITP RDSLKDGDTL SSTDHVFQLG FFSFDQDEQP
     QHRFLCLWYK QPFAVVWVAN RNNPLYGTSG FLNLSAGGDL QLFDGEHRAL WSSSSKATKP
     AKNPYLKINC TGNLLLGDDE EAVLWQSFDD PMNTILAGMK LGKNFKTQQE WSLTSWKTLK
     DPSTGEYTLS LDTRGLPQLI LRKKGDPTYS YRLGSWNGLS FTGAPAMGRE NTLFNYKFTS
     SAQEVNYSWT PRRDIVSRLV LNTTGKLQRF IQSKQHEWNL ANTAPEDECD YYSICGAYAV
     CGISSKNTPS CSCLQGFKPK SGRKWNISRG AEGCVHEVPT KCGKKDIFVK FPGMKLPDTS
     WSWYDSRNAM TLEDCKVKCS STCSCTAYAN TDIRKGGKGC LLWFGDLLDM REYASFGQDV
     YIRMGFAKKE FKGREKVGMI VGSVMSIAVV LVAVFACYRK KIMKRYHGES LIKRVGEENM
     DMGLPILDIK AIYIATDDFS YINFLGRGGF GPVYKGRLEN GQEIAVKRLC ENSGQGVLEF
     KNEVKLIAKL QHRNLVRLLG CCIQGEERML IYEYMPNKSL DFFIFDERRR RELDWGKRSN
     IIYGIARGLL YLHQDSRLRI IHRDLKAGNV LLDNDMNPKI SDFGLAKSFG GDQSESSTNR
     VVGTYGYMPP EYAIDGHFSV KSDVFSFGVL VLEVITGKTN RRFQHADHDL NLLGHVWKLW
     VEDRAIEVPE EDLLEETCAV SEILRCIHVA LLCVQQKPED RPTMASVVLM FGSDGSLPDP
     KQPGFFTNRN VPDVSSSLSR SVNQVSITMI QGR
//
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